2VDA
Solution structure of the SecA-signal peptide complex
Summary for 2VDA
| Entry DOI | 10.2210/pdb2vda/pdb |
| Related | 1M6N 1TF5 1TM6 2FSF |
| Descriptor | TRANSLOCASE SUBUNIT SECA, MALTOPORIN (2 entities in total) |
| Functional Keywords | sugar transport, protein transport, protein targeting, transmembrane, outer membrane, signal peptide, paramagnetic relaxation enhancement, translocase, ion transport, translocation, protein secretion, nucleotide-binding, seca, porin, membrane, transport, atp-binding, high molecular weight complex |
| Biological source | ESCHERICHIA COLI More |
| Cellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10408 Cell outer membrane ; Multi-pass membrane protein : Q8CVI4 |
| Total number of polymer chains | 2 |
| Total formula weight | 96990.49 |
| Authors | Gelis, I.,Bonvin, A.M.J.J.,Keramisanou, D.,Koukaki, M.,Gouridis, G.,Karamanou, S.,Economou, A.,Kalodimos, C.G. (deposition date: 2007-10-01, release date: 2007-11-27, Last modification date: 2018-01-24) |
| Primary citation | Gelis, I.,Bonvin, A.M.J.J.,Keramisanou, D.,Koukaki, M.,Gouridis, G.,Karamanou, S.,Economou, A.,Kalodimos, C.G. Structural Basis for Signal-Sequence Recognition by the Translocase Motor Seca as Determined by NMR Cell(Cambridge,Mass.), 131:756-, 2007 Cited by PubMed: 18022369DOI: 10.1016/J.CELL.2007.09.039 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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